ID ATG1_VANPO Reviewed; 994 AA. AC A7TIZ4; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 16-JUN-2009, entry version 14. DE RecName: Full=Serine/threonine-protein kinase atg1; DE EC=2.7.11.1; DE AltName: Full=Autophagy-related protein 1; GN Name=ATG1; ORFNames=Kpol_541p49; OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) OS (Kluyveromyces polysporus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; OC Vanderwaltozyma. OX NCBI_TaxID=436907; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17494770; DOI=10.1073/pnas.0608218104; RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., RA Wolfe K.H.; RT "Independent sorting-out of thousands of duplicated gene pairs in two RT yeast species descended from a whole-genome duplication."; RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007). CC -!- FUNCTION: Serine/threonine protein kinase probably involved in the CC cytoplasm to vacuole transport (Cvt) and in autophagy, where it CC may be required for the formation of autophagosomes (By CC similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. APG1/unc-51/ULK1 subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS480398; EDO17806.1; -; Genomic_DNA. DR RefSeq; XP_001645664.1; -. DR GeneID; 5546060; -. DR KEGG; vpo:Kpol_541p49; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR017442; Se/Thr_pkinase-rel. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding; Autophagy; Complete proteome; Cytoplasm; Kinase; KW Nucleotide-binding; Protein transport; KW Serine/threonine-protein kinase; Transferase; Transport. FT CHAIN 1 994 Serine/threonine-protein kinase atg1. FT /FTId=PRO_0000317799. FT DOMAIN 7 331 Protein kinase. FT NP_BIND 13 21 ATP (By similarity). FT COMPBIAS 377 525 Asn-rich. FT ACT_SITE 178 178 Proton acceptor (By similarity). FT BINDING 60 60 ATP (By similarity). SQ SEQUENCE 994 AA; 113085 MW; 9BD130D2C810CE81 CRC64; MIISGKYVIE KEIGKGSFAT VLKGYIIDDN DNNGNDTNNE DVEVNDDKRK YTTRNQIAVK AVPRSKLKNK KLLENLEVEI AILKKIKHPH IVRLIECERT STDFYLIMEY CALGDLTFLI KKRQEIMENH PLLKSVFKRF PPPSKNHNGL HRAFILNYLQ QLSSSLKFLR SKNLVHRDIK PQNLLLATPF VDYHDSKSFH DLGYVGISSL PILKIADFGF ARFLPNTSMA ETLCGSPLYM APEILNYQKY NAKADLWSVG TVLYEMCYGK PPFKASNHLE LYKKIKKANN TISYSNDCEI EDDLKDLINA LLTFDPNKRI GFQEFFDNKL VIEDLSKYEV ANEVYSELEL KSKSVLESNM FISEYLPSEK KKDDTDNMII SNLSTNDRIN NITIFSNILP TVNENENDKT NDNSTTNYNN NDNENNDNNN TNHNYNNDKV NNKSNDNNEK SDINRSNSNY KQHSTKQTTN ELIPNTNTIT TNINDNSNSE MNSQSARMMQ KSKNYKSLRN NKLRNSKNDI INNSNSDLIL EKEYVVVEKK SVEVNTLADE MAQIGQINNL NYKVPYPSRS PTLAGNVLQN NESLQHYQPF SVKSPRTSLS SNGSGNSRRA SLVDRRLSIS SLNPSNALSR ALGVASTKLF GSNVLPNQNA GVGNANNINT SMPLLNPQVF QDLTENILLR VDQLQGKDRI NIDSNSIVQI LESLAAKAFV VHSFAEVKFS QTIPLKSLST STVNRPANDR RLNDRGCAIE EDDNIQTETY DTYIPSLKGR SLSSLSQTSI CSQDLPHGEL YQLSKEAIIL YMKTLSILAT AMQITSNWWY QSNEKNCSLR LNLLVQWIRD KFNECLERAD FLRIQILELE ECENKSNELN SDHTDVETSG VNETVHNNDN DANEEDQIYV EKLLYDRALE ISRTAAKLEI QGDHLNNCEL AYATSLWMLE ILLDDRIEDD NFNEFSSKNS AVLDDQDREI IKKYIDSIAN RLKALREKIS QGGS //